Species | Aspergillus niger | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
CAZyme ID | M747DRAFT_293940-t43_1-p1 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | FAD-binding domain-containing protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
223354 | GlcD | 2.87e-20 | 39 | 427 | 65 | 459 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
396238 | FAD_binding_4 | 5.52e-14 | 39 | 139 | 37 | 139 | FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. |
369658 | BBE | 2.02e-10 | 381 | 424 | 1 | 44 | Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. |
215242 | PLN02441 | 2.77e-06 | 44 | 171 | 108 | 242 | cytokinin dehydrogenase |
176879 | START_STARD2_7-like | 0.005 | 339 | 427 | 98 | 184 | Lipid-binding START domain of mammalian STARD2, -7, and related proteins. This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of PtdCho to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers. It showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.97e-294 | 40 | 427 | 86 | 473 | |
6.64e-259 | 40 | 427 | 87 | 474 | |
6.64e-259 | 40 | 427 | 87 | 474 | |
9.25e-259 | 40 | 427 | 96 | 483 | |
5.44e-258 | 40 | 427 | 87 | 474 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.32e-54 | 29 | 427 | 89 | 495 | Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464] |
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2.73e-53 | 40 | 427 | 76 | 472 | Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale] |
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9.90e-52 | 40 | 426 | 82 | 478 | The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum] |
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1.95e-50 | 40 | 426 | 82 | 478 | Chain A, Glucooligosaccharide oxidase [Sarocladium strictum] |
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8.43e-46 | 40 | 426 | 100 | 490 | Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.92e-92 | 42 | 426 | 84 | 469 | FAD-linked oxidoreductase sorD OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=sorD PE=3 SV=1 |
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2.22e-53 | 29 | 427 | 89 | 495 | Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1 |
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2.20e-52 | 40 | 427 | 98 | 494 | Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2 |
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4.72e-51 | 40 | 426 | 101 | 497 | Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1 |
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4.33e-45 | 40 | 426 | 100 | 490 | Chitooligosaccharide oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chitO PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000052 | 0.000000 |
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